title: [Metalloproteinase from Bacillus subtilis: - "intracellular" and extracellular enzymes].
abstract: "Intracellular" metalloproteinase was purified to homogeneity from Bacillus subtilis 103 crude cell extract, using affinity chromatography on bacitracin-Sepharose 4B. The degree of purification and the yield of the enzyme were about 260-fold and 3%, respectively. In its physico-chemical properties and the amino acid composition the enzyme is very similar, if not identical, to the extracellular metalloproteinase isolated from the culture filtrate of the same strain. Extracellular metalloproteinase-deficient mutant strain Bacillus subtilis SMY-512 does not produce the "intracellular" enzyme either. THe activity of "intracellular" metalloproteinase in the periplasmic space of the cells is about 70% of that in the cytoplasm, thus being indicative of a rather regular distribution of the enzyme throughout the cell compartment.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001412:Bacillus subtilis / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D008666:Metalloendopeptidases; D009154:Mutation
chemical_list: D000596:Amino Acids; D010450:Endopeptidases; D008666:Metalloendopeptidases
vernacular_title: Metalloproteinaza iz Bacillus subtilis: vnekletochnyĭ i vnutrikletochnyĭ fermenty.